ID   YGFZ_YERE8              Reviewed;         330 AA.
AC   A1JPM8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN   OrderedLocusNames=YE3387;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Folate-binding protein involved in regulating the level of
CC       ATP-DnaA and in the modification of some tRNAs. It is probably a key
CC       factor in regulatory networks that act via tRNA modification, such as
CC       initiation of chromosomal replication. {ECO:0000255|HAMAP-
CC       Rule:MF_01175}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01175}.
CC   -!- SIMILARITY: Belongs to the tRNA-modifying YgfZ family.
CC       {ECO:0000255|HAMAP-Rule:MF_01175}.
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DR   EMBL; AM286415; CAL13413.1; -; Genomic_DNA.
DR   RefSeq; WP_011817025.1; NC_008800.1.
DR   RefSeq; YP_001007556.1; NC_008800.1.
DR   AlphaFoldDB; A1JPM8; -.
DR   SMR; A1JPM8; -.
DR   STRING; 393305.YE3387; -.
DR   EnsemblBacteria; CAL13413; CAL13413; YE3387.
DR   KEGG; yen:YE3387; -.
DR   PATRIC; fig|393305.7.peg.3595; -.
DR   eggNOG; COG0354; Bacteria.
DR   HOGENOM; CLU_007884_6_1_6; -.
DR   OMA; VNFKKGC; -.
DR   BioCyc; YENT393305:G13HL-3293-MON; -.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009451; P:RNA modification; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01175; tRNA_modifying_YgfZ; 1.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR023758; tRNA-modifying_YgfZ.
DR   InterPro; IPR045179; YgfZ/GcvT.
DR   InterPro; IPR017703; YgfZ/GcvT_CS.
DR   PANTHER; PTHR22602; PTHR22602; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   SUPFAM; SSF101790; SSF101790; 1.
DR   TIGRFAMs; TIGR03317; ygfZ_signature; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Folate-binding; tRNA processing.
FT   CHAIN           1..330
FT                   /note="tRNA-modifying protein YgfZ"
FT                   /id="PRO_1000065780"
FT   BINDING         28
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
FT   BINDING         190
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ   SEQUENCE   330 AA;  36081 MW;  8667DB195047E2FC CRC64;
     MANNTPFAAQ PLLTSSELPL TLISLDDWAL VTLTGADRVK YLQGQVTADI DALPTDQHVL
     CAHCDAKGKM WSNLRLFYRG EGLAFIERRS VLDNQLSELK KYAVFSKVVI AAQPDAVLLG
     VAGTQAKAVL AEVFAELPNA DHPVVQQGDS TLLYFSLPAE RFLLVTDTEQ AQQLVEKLAD
     RAQFNNSKQW LALDIEAGFP IIDTDSSAQF IPQATNIQAL NGISFSKGCY TGQEMVARAK
     YRGANKRALY WLAGSANRAP AVGEDLEWQL GENWRRTGSV LAAITLSDGT VWVQAVLNND
     LAADSVLRVR DDAESVLTIQ PLPYSLTEDK